2.4.1.144	malfunction	detailed glycomic analysis of the effect of GnT-III overexpression in WM266-4-GnT-III metastatic melanoma cells, overview. Overexpression of GnT-III in melanoma leads to modification of a broad range of N-glycan types by the introduction of the bisecting GlcNAc residue with highly branched complex structures among them. The presence of these unusual complex N-glycans results in stronger interactions of cellular glycoproteins with the PHA-L. Elevated activity of GnT-III in cancer cells does not necessarily lead to a total abrogation of the formation of highly branched glycans. The modification of pre-existing N-glycans by the introduction of bisecting GlcNAc can modulate their capacity to interact with carbohydrate-binding proteins such as plant lectins	759316	
2.4.1.144	malfunction	downregulated N-acetylglucosaminyltransferase III is involved in attenuating trophoblast migration and invasion under hypoxia-reoxygenation condition. Excessive oxidative stress can decrease GnT-III expression in trophoblast and the decreased expression of GnT-III may be involved in the development of preeclampsia. Clinical characteristics of preeclampsia group comparedwith normal pregnancy group, overview	759591	
2.4.1.144	malfunction	knockdown of GnT-III by siRNA causes no alteration in expression levels of E-cadherin mRNA and protein, but induces alterations on E-cadherin cellular localization in MCF-7/AZ cells. GnT-III knockdown cells reveal a membrane de-localization of E-cadherin leading to its cytoplasmic accumulation and cause modifications of E-cadherin N-glycans catalyzed by GnT-III and GnT-V	703956	
2.4.1.144	malfunction	suppression of GnT-III in epithelial ovarian carcinoma (EOC) cell lines and primary tumor-derived cells results in an inhibition of Notch signaling that is more potent than pharmacologic blockage of Notch activation via gamma-secretase inhibition. The inhibition results from the redirection of the Notch receptor to the lysosome, a distinct mechanism	759483	
2.4.1.144	metabolism	existence of a bi-directional cross-talk between E-cadherin and two major N-glycan processing enzymes, N-acetylglucosaminyltransferase-III or -V (GnT-III or GnT-V). Molecular mechanisms underlying E-cadherin regulation in gastric cancer, overview	721738	
2.4.1.144	metabolism	GnT-III is considered to be a key glycosyltransferase in the N-glycan biosynthetic pathway because the introduction of the bisecting GlcNAc residue suppresses further processing and elongation of the N-glycans catalyzed by GnT-V. So, in the tumor context, GnT-III and GnT-V have generally a dual role where GnT-III acts as metastases suppressors whereas GnT-V is associated with increased malignancy and metastasis	759591	
2.4.1.144	metabolism	interplay between GnT-III and sialyltransferases in the expression of their enzymatic products and also their functions in tumor metastasis. Interplay between GnT-III and ST6GAL1 in regulating cell migration	736507	
2.4.1.144	metabolism	N-acetylglucosaminyltransferase-III-mediated glycosylation, specifically on E-cadherin, is a major component of the Epithelial-Mesenchymal-Transition /Mesenchymal-Epithelial-Transition mechanism signature	723551	
2.4.1.144	additional information	GnT-III overexpression does not affect cell morphology	721738	
2.4.1.144	additional information	usage of MALDI-TOF and ESIion-trap-MS/MS together with HILIC-HPLC of 2-AA labeled N-glycans to study the N-glycome of membrane-attached and secreted proteins. Characterization of N-glycan epitopes on membrane and secreted proteins using plant lectins, several plant lectins are used in lectin blot assay, overview	759316